DB code: M00178

RLCP classification 3.113.90000.397 : Transfer
3.1103.6090.130 : Transfer
CATH domain 2.40.240.10 : Ribosomal Protein L25; Chain P
2.40.240.10 : Ribosomal Protein L25; Chain P
1.10.1160.10 : Glutamyl-tRNA Synthetase; domain 2 Catalytic domain
3.90.800.10 : Glutamyl-tRNA Synthetase; domain 3
3.40.50.620 : Rossmann fold Catalytic domain
E.C. 6.1.1.18
CSA 1euy
M-CSA 1euy
MACiE

CATH domain Related DB codes (homologues)
3.40.50.620 : Rossmann fold S00314 S00549 S00316 S00317 S00318 S00315 T00085 T00249 D00300 M00177 T00106 T00114

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P00962 Glutaminyl-tRNA synthetase
EC 6.1.1.18
Glutamine--tRNA ligase
GlnRS
NP_415206.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_488960.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00749 (tRNA-synt_1c)
PF03950 (tRNA-synt_1c_C)
[Graphical View]

KEGG enzyme name
glutamine---tRNA ligase
glutaminyl-tRNA synthetase
glutaminyl-transfer RNA synthetase
glutaminyl-transfer ribonucleate synthetase
glutamine-tRNA synthetase
glutamine translase
glutamate-tRNA ligase
glutaminyl ribonucleic acid
GlnRS

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00962 SYQ_ECOLI ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). Monomer. Cytoplasm.

KEGG Pathways
Map code Pathways E.C.
MAP00251 Glutamate metabolism
MAP00970 Aminoacyl-tRNA biosynthesis

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C00064 C01640 C00020 C00013 C02282
E.C.
Compound Magnesium ATP L-Glutamine tRNA(Gln) AMP Pyrophosphate L-Glutaminyl-tRNA(Gln) Glutaminyl-adenylate
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide amino acids,amide group nucleic acids amine group,nucleotide phosphate group/phosphate ion amino acids,amide group,nucleic acids
ChEBI 18420
18420
15422
15422
18050
58359
18050
58359
16027
16027
29888
29888
PubChem 888
888
5957
5957
5961
6992086
5961
6992086
6083
6083
1023
21961011
1023
21961011
1euqA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euyA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1exdA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gsgP01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtrA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtsA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1nylA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0bA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0cA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrsA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrtA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qruA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qtqA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1zjwA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euqA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euyA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1exdA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gsgP02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtrA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtsA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1nylA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0bA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0cA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrsA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrtA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qruA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qtqA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1zjwA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euqA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euyA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1exdA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gsgP03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtrA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtsA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1nylA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0bA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0cA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrsA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrtA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qruA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qtqA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1zjwA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euqA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euyA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1exdA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gsgP04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtrA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1gtsA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1nylA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0bA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0cA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrsA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qrtA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qruA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qtqA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1zjwA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1euqA05 Unbound Unbound Unbound Bound:G-C-C-A_976 (chain B:3'-terminus) Unbound Unbound Unbound Intermediate-analogue:QSI
1euyA05 Unbound Unbound Unbound Bound:G-C-C-A_976 (chain B:3'-terminus) Unbound Unbound Unbound Intermediate-analogue:QSI
1exdA05 Unbound Unbound Unbound Bound:G-C-C-A_976 (chain B:3'-terminus) Analogue:__A Unbound Unbound Unbound
1gsgP05 Unbound Unbound Unbound Bound:G-C-C-A_76 (chain T:3'-terminus) Unbound Unbound Unbound Unbound
1gtrA05 Unbound Bound:ATP Unbound Bound:G-C-C-A_76 (chain B:3'-terminus) Unbound Unbound Unbound Unbound
1gtsA05 Unbound Unbound Unbound Bound:G-C-C-A_76 (chain B:3'-terminus) Bound:AMP Unbound Unbound Unbound
1nylA05 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1o0bA05 Unbound Unbound Bound:GLN Bound:G-C-C-A_976 (chain B:3'-terminus) Analogue:AMP Analogue:SO4_1394 Unbound Unbound
1o0cA05 Unbound Unbound Analogue:GLU Bound:G-C-C-A_976 (chain B:3'-terminus) Bound:AMP Analogue:SO4_1394 Unbound Unbound
1qrsA05 Unbound Bound:ATP Unbound Bound:G-C-C-A_76 (chain B:3'-terminus) Unbound Unbound Unbound Unbound
1qrtA05 Unbound Bound:ATP Unbound Bound:G-C-C-A_76 (chain B:3'-terminus) Unbound Unbound Unbound Unbound
1qruA05 Unbound Bound:ATP Unbound Bound:G-C-C-A_76 (chain B:3'-terminus) Unbound Unbound Unbound Unbound
1qtqA05 Unbound Unbound Unbound Bound:G-C-C-A_976 (chain B:3'-terminus) Unbound Analogue:SO4_1394 Unbound Intermediate-analogue:QSI
1zjwA05 Unbound Unbound Bound:GLN Analogue:G-C-C-A_976 (chain B:3'-terminus) Bound:AMP Analogue:SO4_1394 Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [33]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1euqA01
1euyA01
1exdA01
1gsgP01
1gtrA01
1gtsA01
1nylA01
1o0bA01
1o0cA01
1qrsA01
1qrtA01
1qruA01
1qtqA01
1zjwA01
1euqA02
1euyA02
1exdA02
1gsgP02
1gtrA02
1gtsA02
1nylA02
1o0bA02
1o0cA02
1qrsA02
1qrtA02
1qruA02
1qtqA02
1zjwA02
1euqA03 ARG 260;LYS 270
1euyA03 ARG 260;LYS 270
1exdA03 ARG 260;LYS 270
1gsgP03 ARG 260;LYS 270
1gtrA03 ARG 260;LYS 270
1gtsA03 ARG 260;LYS 270
1nylA03 ARG 260;LYS 270
1o0bA03 ARG 260;LYS 270
1o0cA03 ARG 260;LYS 270
1qrsA03 ARG 260;LYS 270
1qrtA03 ARG 260;LYS 270
1qruA03 ARG 260;LYS 270
1qtqA03 ARG 260;LYS 270
1zjwA03 ARG 260;LYS 270
1euqA04
1euyA04
1exdA04
1gsgP04
1gtrA04
1gtsA04
1nylA04
1o0bA04
1o0cA04
1qrsA04
1qrtA04
1qruA04
1qtqA04
1zjwA04
1euqA05 GLU 34;ASN 36;HIS 43 GLU 34
1euyA05 GLU 34;ASN 36;HIS 43 GLU 34
1exdA05 GLU 34;ASN 36;HIS 43 GLU 34
1gsgP05 GLU 34;ASN 36;HIS 43 GLU 34
1gtrA05 GLU 34;ASN 36;HIS 43 GLU 34
1gtsA05 GLU 34;ASN 36;HIS 43 GLU 34
1nylA05 GLU 34;ASN 36;HIS 43 GLU 34
1o0bA05 GLU 34;ASN 36;HIS 43 GLU 34
1o0cA05 GLU 34;ASN 36;HIS 43 GLU 34
1qrsA05 GLU 34;ASN 36;HIS 43 GLU 34 mutant D235G
1qrtA05 GLU 34;ASN 36;HIS 43 GLU 34 mutant D235G
1qruA05 GLU 34;ASN 36;HIS 43 GLU 34
1qtqA05 GLU 34;ASN 36;HIS 43 GLU 34
1zjwA05 GLU 34;ASN 36;HIS 43 GLU 34

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[10]
Fig.13, p.8768-8771
[33]
Fig.9, p.446-447 2

References
[1]
Resource
Comments
Medline ID
PubMed ID 2459391
Journal J Mol Biol
Year 1988
Volume 202
Pages 121-6
Authors Perona JJ, Swanson R, Steitz TA, Soll D
Title Overproduction and purification of Escherichia coli tRNA(2Gln) and its use in crystallization of the glutaminyl-tRNA synthetase-tRNA(Gln) complex.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2686030
Journal Science
Year 1989
Volume 246
Pages 1152-4
Authors Perona JJ, Swanson RN, Rould MA, Steitz TA, Soll D
Title Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
Medline ID 90069584
PubMed ID 2479982
Journal Science
Year 1989
Volume 246
Pages 1135-42
Authors Rould MA, Perona JJ, Soll D, Steitz TA
Title Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution.
Related PDB 1gsg
Related UniProtKB P00962
[4]
Resource
Comments
Medline ID
PubMed ID 2194108
Journal Mol Biol Rep
Year 1990
Volume 14
Pages 213-4
Authors Steitz TA, Rould MA, Perona JJ
Title Structural basis of tRNA discrimination as derived from the high resolution crystal structure of glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 1915346
Journal Eur J Biochem
Year 1991
Volume 200
Pages 739-45
Authors Bhattacharyya T, Bhattacharyya A, Roy S
Title A fluorescence spectroscopic study of glutaminyl-tRNA synthetase from Escherichia coli and its implications for the enzyme mechanism.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1857423
Journal Nature
Year 1991
Volume 352
Pages 258-60
Authors Jahn M, Rogers MJ, Soll D
Title Anticodon and acceptor stem nucleotides in tRNA(Gln) are major recognition elements for E. coli glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID 91312443
PubMed ID 1857417
Journal Nature
Year 1991
Volume 352
Pages 213-8
Authors Rould MA, Perona JJ, Steitz TA
Title Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase.
Related PDB 1gtr
Related UniProtKB P00962
[8]
Resource
Comments
Medline ID
PubMed ID 2011598
Journal Proc Natl Acad Sci U S A
Year 1991
Volume 88
Pages 2903-7
Authors Perona JJ, Rould MA, Steitz TA, Risler JL, Zelwer C, Brunie S
Title Structural similarities in glutaminyl- and methionyl-tRNA synthetases suggest a common overall orientation of tRNA binding.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 8369295
Journal Biochemistry
Year 1993
Volume 32
Pages 9268-73
Authors Bhattacharyya T, Roy S
Title A fluorescence spectroscopic study of substrate-induced conformational changes in glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[10]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8364025
Journal Biochemistry
Year 1993
Volume 32
Pages 8758-71
Authors Perona JJ, Rould MA, Steitz TA
Title Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase.
Related PDB 1gts
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 7515283
Journal Biochimie
Year 1993
Volume 75
Pages 1051-60
Authors Dyson MR, Mandal N, RajBhandary UL
Title Relationship between the structure and function of Escherichia coli initiator tRNA.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 8199248
Journal Biochimie
Year 1993
Volume 75
Pages 1125-36
Authors McClain WH, Schneider J, Gabriel K
Title Association of tRNA(Gln) acceptor identity with phosphate-sugar backbone interactions observed in the crystal structure of the Escherichia coli glutaminyl-tRNA synthetase-tRNA(Gln) complex.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 8199243
Journal Biochimie
Year 1993
Volume 75
Pages 1083-90
Authors Rogers MJ, Weygand-Durasevic I, Schwob E, Sherman JM, Rogers KC, Adachi T, Inokuchi H, Soll D
Title Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 7505222
Journal EMBO J
Year 1993
Volume 12
Pages 5201-8
Authors Schwob E, Soll D
Title Selection of a 'minimal' glutaminyl-tRNA synthetase and the evolution of class I synthetases.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 8360919
Journal J Mol Evol
Year 1993
Volume 37
Pages 5-10
Authors Di Giulio M
Title Origin of glutaminyl-tRNA synthetase: an example of palimpsest?
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 7680483
Journal Proc Natl Acad Sci U S A
Year 1993
Volume 90
Pages 2010-4
Authors Weygand-Durasevic I, Schwob E, Soll D
Title Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 8011621
Journal Biochemistry
Year 1994
Volume 33
Pages 7560-7
Authors Arnez JG, Steitz TA
Title Crystal structure of unmodified tRNA(Gln) complexed with glutaminyl-tRNA synthetase and ATP suggests a possible role for pseudo-uridines in stabilization of RNA structure.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 8027995
Journal J Mol Biol
Year 1994
Volume 240
Pages 111-8
Authors Weygand-Durasevic I, Rogers MJ, Soll D
Title Connecting anticodon recognition with the active site of Escherichia coli glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 7506418
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 291-5
Authors Rogers MJ, Adachi T, Inokuchi H, Soll D
Title Functional communication in the recognition of tRNA by Escherichia coli glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 8643392
Journal Nucleic Acids Symp Ser
Year 1995
Volume (33)
Pages 40-2
Authors Ibba M, Thomann HU, Hong KW, Sherman JM, Weygand-Durasevic I, Sever S, Stange-Thomann N, Praetorius M, Soll D
Title Substrate selection by aminoacyl-tRNA synthetases.
Related PDB
Related UniProtKB
[21]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8942633
Journal Biochemistry
Year 1996
Volume 35
Pages 14725-33
Authors Arnez JG, Steitz TA
Title Crystal structures of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP.
Related PDB 1qrs 1qrt 1qru
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 8555233
Journal Biochemistry
Year 1996
Volume 35
Pages 601-7
Authors Sherman JM, Soll D
Title Aminoacyl-tRNA synthetases optimize both cognate tRNA recognition and discrimination against noncognate tRNAs.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 8601833
Journal J Mol Biol
Year 1996
Volume 256
Pages 818-28
Authors Sherman JM, Thomann HU, Soll D
Title Functional connectivity between tRNA binding domains in glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 8917315
Journal Mol Gen Genet
Year 1996
Volume 252
Pages 717-22
Authors Kitabatake M, Ibba M, Hong KW, Soll D, Inokuchi H
Title Genetic analysis of functional connectivity between substrate recognition domains of Escherichia coli glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 8692925
Journal Proc Natl Acad Sci U S A
Year 1996
Volume 93
Pages 6953-8
Authors Ibba M, Hong KW, Sherman JM, Sever S, Soll D
Title Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme.
Related PDB
Related UniProtKB
[26]
Resource
Comments
Medline ID
PubMed ID 9372179
Journal Biol Chem
Year 1997
Volume 378
Pages 1103-17
Authors Freist W, Gauss DH, Ibba M, Soll D
Title Glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 9185564
Journal Nucleic Acids Res
Year 1997
Volume 25
Pages 2562-5
Authors Lustig B, Arora S, Jernigan RL
Title RNA base-amino acid interaction strengths derived from structures and sequences.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 9657697
Journal Biochemistry
Year 1998
Volume 37
Pages 9836-42
Authors Liu J, Ibba M, Hong KW, Soll D
Title The terminal adenosine of tRNA(Gln) mediates tRNA-dependent amino acid recognition by glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 9799245
Journal EMBO J
Year 1998
Volume 17
Pages 6377-84
Authors Stoldt M, Wohnert J, Gorlach M, Brown LR
Title The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 9746349
Journal Eur J Biochem
Year 1998
Volume 256
Pages 80-7
Authors Siatecka M, Rozek M, Barciszewski J, Mirande M
Title Modular evolution of the Glx-tRNA synthetase family--rooting of the evolutionary tree between the bacteria and archaea/eukarya branches.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 9738468
Journal FEBS Lett
Year 1998
Volume 434
Pages 149-54
Authors Hong KW, Ibba M, Soll D
Title Retracing the evolution of amino acid specificity in glutaminyl-tRNA synthetase.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 9568911
Journal Protein Sci
Year 1998
Volume 7
Pages 1046-51
Authors Mandal AK, Bhattacharyya A, Bhattacharyya S, Bhattacharyya T, Roy S
Title A cognate tRNA specific conformational change in glutaminyl-tRNA synthetase and its implication for specificity.
Related PDB
Related UniProtKB
[33]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
Medline ID 98230743
PubMed ID 9562563
Journal Structure
Year 1998
Volume 6
Pages 439-49
Authors Rath VL, Silvian LF, Beijer B, Sproat BS, Steitz TA
Title How glutaminyl-tRNA synthetase selects glutamine.
Related PDB 1qtq
Related UniProtKB P00962
[34]
Resource
Comments
Medline ID
PubMed ID 10801842
Journal J Biol Chem
Year 2000
Volume 275
Pages 21768-72
Authors Kim T, Park SG, Kim JE, Seol W, Ko YG, Kim S
Title Catalytic peptide of human glutaminyl-tRNA synthetase is essential for its assembly to the aminoacyl-tRNA synthetase complex.
Related PDB
Related UniProtKB
[35]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID 20318776
PubMed ID 10860750
Journal J Mol Biol
Year 2000
Volume 299
Pages 431-46
Authors Sherlin LD, Bullock TL, Newberry KJ, Lipman RS, Hou YM, Beijer B, Sproat BS, Perona JJ
Title Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.
Related PDB 1euq 1euy
Related UniProtKB P00962
[36]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10881199
Journal Nat Struct Biol
Year 2000
Volume 7
Pages 497-504
Authors Bullock TL, Sherlin LD, Perona JJ
Title Tertiary core rearrangements in a tight binding transfer RNA aptamer.
Related PDB 1exd
Related UniProtKB
[37]
Resource
Comments
Medline ID
PubMed ID 11224555
Journal Nat Struct Biol
Year 2001
Volume 8
Pages 189-91
Authors Francklyn CS
Title Charging two for the price of one.
Related PDB
Related UniProtKB
[38]
Resource
Comments
Medline ID
PubMed ID 11724963
Journal Proc Natl Acad Sci U S A
Year 2001
Volume 98
Pages 14244-9
Authors Patzelt H, Rudiger S, Brehmer D, Kramer G, Vorderwulbecke S, Schaffitzel E, Waitz A, Hesterkamp T, Dong L, Schneider-Mergener J, Bukau B, Deuerling E
Title Binding specificity of Escherichia coli trigger factor.
Related PDB
Related UniProtKB
[39]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12691748
Journal J Mol Biol
Year 2003
Volume 328
Pages 395-408
Authors Bullock TL, Uter N, Nissan TA, Perona JJ
Title Amino acid discrimination by a class I aminoacyl-tRNA synthetase specified by negative determinants.
Related PDB 1o0b 1o0c
Related UniProtKB
[40]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12737824
Journal Structure (Camb)
Year 2003
Volume 11
Pages 591-603
Authors Sherlin LD, Perona JJ
Title tRNA-dependent active site assembly in a class I aminoacyl-tRNA synthetase.
Related PDB 1nyl
Related UniProtKB
[41]
Resource
Comments
Medline ID
PubMed ID 15845536
Journal J Biol Chem
Year 2005
Volume 280
Pages 23978-86
Authors Gruic-Sovulj I, Uter N, Bullock T, Perona JJ
Title tRNA-dependent aminoacyl-adenylate hydrolysis by a nonediting class I aminoacyl-tRNA synthetase.
Related PDB 1zjw
Related UniProtKB

Comments
According to literature [26], this enzyme utilizes magnesium ion as a cofactor, which is bound to beta- and gamma-phosphate groups of ATP, without any interaction with enzyme residues.
This enzyme catalyzes two successive transfer reactions, a phosphoryl transfer, and an acyl transfer. According to the literature [10] & [33], the catalytic reactions proceed as follows:
(A) Transfer of adenylate from ATP to carboxyl oxygen of glutamine substrate:
(A1) The carboxylate oxygen makes a nucleophilic attack on the transferred group, alpha-phosphate group of ATP, forming a pentacovalent transtion-state.
(A2) The transferred group is stabilized by mainchain amide of Glu34, sidechains of His43 and Lys270, whereas the leaving beta- and gamma-phosphate groups are stabilized by the cofactor, magnesium ion, along with sidechains of Lys270 and Asn36.
(A3) This reaction gives glutaminyl-adenylate intermediate and pyrophosphate. (SN2-like reaction)
(B) Transfer of acyl group from glutaminyl-adenylate intermediate to 2'-OH of 3'-terminus of tRNA:
(B1) Glu34 acts as a general base to deprotonate the acceptor group, 2'-OH group of tRNA ribose.
(B2) The activated acceptor group, 2'-hydroxyl oxygen makes a nucleophilic attack on the transferred acyl group (carbonyl carbon) of the intermediate.
(B3) The transferred group, acyl group, gives an oxyanion tetrahedral intermediate with negative charge. This negatively charge will probably be stabilized by Arg260, through a water molecule (see [33]). The leaving phosphate group of AMP is stabilized by mainchain amide of Glu34 and sidechains of His43 and Lys270.
(B4) Finally, covalent bond between 2'-oxygen and acyl group is formed, with release of AMP.

Created Updated
2004-09-14 2009-02-26